ID   EX7L_BACC7              Reviewed;         452 AA.
AC   B7HNU3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378};
GN   OrderedLocusNames=BCAH187_A4310;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC       insoluble oligonucleotides, which are then degraded further into small
CC       acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC         direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00378};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00378}.
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DR   EMBL; CP001177; ACJ80682.1; -; Genomic_DNA.
DR   RefSeq; WP_000415266.1; NC_011658.1.
DR   AlphaFoldDB; B7HNU3; -.
DR   SMR; B7HNU3; -.
DR   EnsemblBacteria; ACJ80682; ACJ80682; BCAH187_A4310.
DR   GeneID; 59155246; -.
DR   GeneID; 64199530; -.
DR   KEGG; bcr:BCAH187_A4310; -.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000002214; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
DR   GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04489; ExoVII_LU_OBF; 1.
DR   HAMAP; MF_00378; Exonuc_7_L; 1.
DR   InterPro; IPR003753; Exonuc_VII_L.
DR   InterPro; IPR020579; Exonuc_VII_lsu_C.
DR   InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR   PANTHER; PTHR30008; PTHR30008; 1.
DR   Pfam; PF02601; Exonuc_VII_L; 1.
DR   Pfam; PF13742; tRNA_anti_2; 1.
DR   TIGRFAMs; TIGR00237; xseA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN           1..452
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000122041"
SQ   SEQUENCE   452 AA;  51368 MW;  567F37FA7A57846E CRC64;
     MEKQYLTVTA LTRYIKTKIE YDPHLQSVWL KGEISNFKNH SRGHMYFTLK DENARIAAVM
     FAGHNRNIKF RPENGMKVLV KGKISVYEAS GSYQIYIQDM QPDGVGNLHL AYEQLKVRLE
     EEGLFSQVYK KTIPPYAKTI GVITSPTGAA IRDIITTIKR RYPIGNVIVF PVLVQGESAA
     PSIVQAIRTA NEMEGIDVLI VGRGGGSIEE LWAFNEEMVA RAIFKSEIPI ISAVGHETDF
     TIADFVADLR APTPTAAAEL AAPNIIELQE KVLQRTLRLQ RAMRELVHKK EEKLQVLQKS
     YAFRYPRQVY EQKEEQLDRA LEQLVLAKER YIDKKVNQLK QLSFYLEKHH PSQKIMQTKV
     AVETLQKQLQ REMQTLLQTK EFAFVRAAQK LEALSPLKVM MRGYGLVYDE EKQVLKSVKD
     VSLGDAVSVQ LQDGILDCSV SGIEERELNN GK